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An extracellular enzyme with hyaluronidase and chondroitinase activities from some oral anaerobic spirochaetes

D. Scott^1,3,

Departments of Microbiology and Immunology, Faculty of Medicine, McGill University, Montreal, Quebec, Canada
Department of Oral Biology, Faculty of Dentistry, McGill University, Montreal, Quebec, Canada

³Author for correspondence: D. Scott. Tel: +44 1232 240503 ext. 3515. Fax: +44 1232 438861.

ABSTRACT

Treponema denticola, Treponema vincentii and Treponema socranskii produce an enzyme that hydrolyses hyaluronic acid (HA) and chondroitin sulphate (CS). The secreted enzyme is specifically inhibited by gold sodium thiomalate and anti-bee-venom antibodies. The use of saturated substrate (HA or CS) transblots allowed the visualization of active enzyme directly from culture supernatants and is a useful tool in clarification of complex polysaccharide-degrading enzyme specificities. The affinity-purified extracellular enzyme of T. denticola contains a single molecular species with a molecular mass of 59 kDa. Since it hydrolyses both HA and CS, it can more appropriately be termed a hyaluronoglucosaminidase (HGase). The HGase has been localized at the cell surface by electron microscopy and may play an active role in the degradation of connective tissue ground substance in the initiation and progression of periodontal disease.

Present address: School of Dentistry, Queen's University of Belfast, Grosvenor Road, Belfast BT12 6BP, UK.

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